Physicochemical and structural properties of amaranth protein isolates treated with high pressure

Relationship between protein characteristics and film‐forming properties of kidney bean, field pea and amaranth protein isolates

“…Such exposed groups may interact via both covalent (disulphide bonds) and noncovalent interactions to form high Mw aggregates. Similar high Mw fractions attributing to protein aggregates have been reported earlier in protein isolates from Mediterranean legumes (Pastor‐Cavada et al ., ) and amaranth protein isolates (Condes et al ., ).…”

Effect of maleylation on physicochemical and functional properties of rapeseed protein isolate

“…This suggests either deacylation of SH in presence of high MA (Groninger and Miller 1979) or acylation-induced exposure of inaccessible thiol groups initially buried within the hydrophobic interior (mainly by protein unfolding and/or subsequent dissociation) has occurred. It should be pointed out that higher degree of unfolding and dissociation of protein molecules intensifies hydrophobic interactions, which in-turn favours the generation of S-S bonds (Condés et al 2012). This might account for the overall marginal rise in S-S linkage as-well (Fig.…”

“…Such dissociation followed by re-aggregation has been reported in a number of oilseed proteins. In addition, there is also a possibility that introduction of acyl groups may slightly expand the subunits, making them to change their hydrodynamic radii, so that their characteristic peaks would shift or appear at different retention time (Condés et al 2012). Upon exhaustive acylation (≥0.6MA), the relative proportion of 6 and 3.8 kDa fractions were distinctly increased at the expense of 13 kDa peak which finally disappeared at 0.8MA.…”

Amaranth protein films prepared with high-pressure treated proteins

“…Furthermore it has been reported that some of these modified proteins, showed a remarkable improvement in their functionality for example, in its ability to form and stabilize foams, emulsions and gels (Bouaouina et al, 2006;Speroni et al, 2009;Puppo et al, 2005). Condés et al (2012) has reported that amaranth isolate proteins were very sensitive to HP treatment, more than others such as soybean proteins, since they suffered a higher degree of denaturation at 200 and 400 MPa, which was accompanied by a decrease in protein solubility and protein dissociation and aggregation via hydrophobic interactions and disulfide bonds.…”

“…Considering that amaranth protein didn't gel during high-pressure treatment at protein concentrations of filmogenic dispersions (%5% w/v) (Condés et al, 2012) and that large volumes of sample could be handled by HP, protein modification may be carried out on film forming dispersions, avoiding having to lyophilize and redisolve proteins (as was necessary with heat-treated proteins), what would be a major advantage in processing.…”